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- W2810135452 endingPage "91" @default.
- W2810135452 startingPage "71" @default.
- W2810135452 abstract "Intracellular protein homeostasis is largely controlled by Heat shock proteins (Hsp). Heat shock proteins (Hsp) impart an age-old defense mechanism for all forms of life on earth. Misfolded proteins are refolded with the aid of Hsp and proteins which are damaged beyond repair are eliminated with assistance from Hsp. Hsp are known as molecular chaperones for their cytoprotective roles. In cancer cells the Hsp are frequently overexpressed and are assumed to be associated with tumor formation. Hsp demonstrate specific affinity to particular classes of oncogenic peptides and client proteins in cancer cells, and are able to stabilize mutated oncogene proteins. They play a key regulatory role in prevention of apoptotic cell death during tumorigenesis and thereby enhance cell growth and proliferation. They may also promote chemoresistance in cancer cells. Here we present the current knowledge on the role of molecular chaperones in particular heat shock protein 70 (Hsp70) in human gastrointestinal cancers along with their therapeutic targeting. This review will focus on the role of Hsp 70 and related chaperones in several gastrointestinal cancers such as pancreatic, gastric, and liver cancers." @default.
- W2810135452 created "2018-07-10" @default.
- W2810135452 creator A5039842795 @default.
- W2810135452 creator A5075658352 @default.
- W2810135452 creator A5076505686 @default.
- W2810135452 creator A5079990400 @default.
- W2810135452 creator A5080994539 @default.
- W2810135452 creator A5089313929 @default.
- W2810135452 date "2018-01-01" @default.
- W2810135452 modified "2023-09-23" @default.
- W2810135452 title "Involvement of Heat Shock Protein 70 (Hsp70) in Gastrointestinal Cancers" @default.
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